ID W7F7S4_PLAF8 Unreviewed; 570 AA.
AC W7F7S4;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=aspartyl aminopeptidase {ECO:0000256|ARBA:ARBA00011965};
DE EC=3.4.11.21 {ECO:0000256|ARBA:ARBA00011965};
GN ORFNames=PFBG_02677 {ECO:0000313|EMBL:EUR72175.1};
OS Plasmodium falciparum (isolate 7G8).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=57266 {ECO:0000313|EMBL:EUR72175.1, ECO:0000313|Proteomes:UP000030688};
RN [1] {ECO:0000313|Proteomes:UP000030688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7G8 {ECO:0000313|Proteomes:UP000030688};
RG The Broad Institute Genome Sequencing Platform;
RA Volkman S.K., Daily J.P., Sarr O., Ndiaye D., Ndir O., Mboup S., Lukens A.,
RA Stange-Thomann N., Mauceli E., Gnerre S., Jaffe D., Zainoun J.,
RA Wiegand R.C., Birren B., Galagan J., Lander E., Wirth D.F.;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EUR72175.1, ECO:0000313|Proteomes:UP000030688}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=7G8 {ECO:0000313|EMBL:EUR72175.1,
RC ECO:0000313|Proteomes:UP000030688};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Neafsey D., Cheeseman I., Volkman S., Adams J., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Plasmodium falciparum 7G8.";
RL Submitted (FEB-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of an N-terminal aspartate or glutamate from a
CC peptide, with a preference for aspartate.; EC=3.4.11.21;
CC Evidence={ECO:0000256|ARBA:ARBA00001335};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|ARBA:ARBA00001947};
CC -!- SIMILARITY: Belongs to the peptidase M18 family.
CC {ECO:0000256|ARBA:ARBA00008290, ECO:0000256|RuleBase:RU004386}.
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DR EMBL; KE123613; EUR72175.1; -; Genomic_DNA.
DR AlphaFoldDB; W7F7S4; -.
DR SMR; W7F7S4; -.
DR EnsemblProtists; EUR72175; EUR72175; PFBG_02677.
DR VEuPathDB; PlasmoDB:Pf7G8_090037400; -.
DR Proteomes; UP000030688; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd05658; M18_DAP; 1.
DR Gene3D; 2.30.250.10; Aminopeptidase i, Domain 2; 1.
DR Gene3D; 3.40.630.10; Zn peptidases; 1.
DR InterPro; IPR001948; Peptidase_M18.
DR InterPro; IPR023358; Peptidase_M18_dom2.
DR PANTHER; PTHR28570; ASPARTYL AMINOPEPTIDASE; 1.
DR PANTHER; PTHR28570:SF3; ASPARTYL AMINOPEPTIDASE; 1.
DR Pfam; PF02127; Peptidase_M18; 2.
DR PRINTS; PR00932; AMINO1PTASE.
DR SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|RuleBase:RU004386};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU004386};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004386};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049,
KW ECO:0000256|RuleBase:RU004386};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU004386};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|RuleBase:RU004386}.
SQ SEQUENCE 570 AA; 65635 MW; A87094CCC675BF1C CRC64;
MDKKAREYAQ DALKFIQRSG SNFLACKNLK ERLENNGFIN LSEGETWNLN KNEGYVLCKE
NRNICGFFVG KNFNIDTGSI LISIGHIDSC ALKISPNNNV IKKKIHQINV ECYGSGLWHT
WFDRSLGLSG QVLYKKGNKL VEKLIQINKS VLFLPSLAIH LQNRTRYDFS VKINYENHIK
PIISTTLFNQ LNKCKRNNVH HDTILTTDTK FSHKENSQNK RDDQMCHSFN DKDVSNHNLD
KNTIEHLTNQ QNEEKNKHTK DNPNSKDIVE HINTDNSYPL LYLLSKELNC KEEDILDFEL
CLMDTQEPCF TGVYEEFIEG ARFDNLLGSF CVFEGFIELV NSIKNHTSNE NTNHTNNITN
DINDNIHNNL YISIGYDHEE IGSLSEVGAR SYCTKNFIDR IISSVFKKEI HEKNLSVQEI
YGNLVNRSFI LNVDMAHCSH PNYPETVQDN HQLFFHEGIA IKYNTNKNYV TSPLHASLIK
RTFELYYNKY KQQIKYQNFM VKNDTPCGST VGSMVAANLS MPGIDIGIPQ LAMHSIREIA
AVHDVFFLIK GVFAFYTYYN QVLSTCVHDK
//